Co-exposure to deltamethrin and thiacloprid induces cytotoxicity and oxidative stress in human lung cells

2020 ◽  
Vol 36 (11) ◽  
pp. 916-924
Author(s):  
Vedat Şekeroğlu ◽  
Alperen Karabıyık ◽  
Zülal Atlı Şekeroğlu
Keyword(s):  
Oxidative Stress ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Limited Information ◽  
Human Telomerase Reverse Transcriptase ◽  
Human Lung Fibroblast ◽  
Human Lung Fibroblasts ◽  
Human Lung Cells ◽  
Human Telomerase ◽  
And Oxidative Stress

Deltamethrin (DEL) and thiacloprid (THIA) are commonly used synthetic insecticides in agriculture either separately or in combination. There is limited information in human cells for the effects of the mixture of DEL + THIA on oxidative stress. Therefore, the present study was designed to examine the effects of the mixture on cell proliferation and oxidative stress in human lung fibroblast cells. Human telomerase reverse transcriptase (hTERT)-expressing human lung fibroblasts, WTHBF-6 cells, were treated with 2.5 + 37.5, 5 + 75, 12.5 + 187.5, and 25 +375 µM concentrations of DEL + THIA for the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide assay and 5 + 75, 12.5 + 187.5, and 25 + 375 µM for lipid peroxidation and reduced glutathione (GSH) assays for 24, 48, and 72 h in the absence and presence of metabolizing fractions of the mammalian liver (S9 mixture). Both the mixture of DEL + THIA and their metabolites significantly reduced cell viability and induced cytotoxicity in WTHBF-6 cells, especially at higher concentrations. The mixture of DEL + THIA significantly decreased GSH levels at the highest concentration for all treatment times and at the highest two concentrations (12.5 + 187.5 and 25 + 375 µM) for 72 h in the presence of S9 mixture. The highest concentration of DEL + THIA mixture caused a significant increase in malondialdehyde (MDA) level at 72 h in the absence of S9 mixture. There were also significant increases in MDA levels at the highest concentration for 48-h and all concentrations of DEL + THIA for 72-h treatment in WTHBF-6 cell cultures with S9. These data showed that the mixture of DEL + THIA and their metabolites can induce cytotoxicity and oxidative stress in human lung fibroblasts.

scholarly journals Catechin and epicatechin reduce mitochondrial dysfunction and oxidative stress induced by amiodarone in human lung fibroblasts

2017 ◽  
Vol 33 (3) ◽  
pp. 220-225 ◽  
Author(s):  
Luciana Fernandes Silva Santos ◽  
Adriana Stolfo ◽  
Caroline Calloni ◽  
Mirian Salvador
Keyword(s):  
Oxidative Stress ◽  
Mitochondrial Dysfunction ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Human Lung Fibroblasts ◽  
And Oxidative Stress

scholarly journals Cigarette smoke-induced expression of heme oxygenase-1 in human lung fibroblasts is regulated by intracellular glutathione

2008 ◽  
Vol 295 (4) ◽  
pp. L624-L636 ◽  
Author(s):  
Carolyn J. Baglole ◽  
Patricia J. Sime ◽  
Richard P. Phipps
Keyword(s):  
Cigarette Smoke ◽  
Heme Oxygenase ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Nuclear Accumulation ◽  
Heme Oxygenase 1 ◽  
Induced Expression ◽  
Human Lung Fibroblast ◽  
Human Lung Fibroblasts ◽  
Intracellular Glutathione

Fibroblasts are key structural cells that can be damaged by cigarette smoke. Cigarette smoke contains many components capable of eliciting oxidative stress, which may induce heme oxygenase (HO)-1, a cytoprotective enzyme. There are no data on HO-1 expression in primary human lung fibroblasts after cigarette smoke extract (CSE) exposure. We hypothesized that human lung fibroblasts exposed to cigarette smoke would increase HO-1 though changes in intracellular glutathione (GSH). Primary human lung fibroblasts were exposed to CSE, and changes in HO-1 expression and GSH levels were assessed. CSE induced a time- and dose-dependent increase in expression of HO-1, but not HO-2 or biliverdin reductase, in two different primary human lung fibroblast strains, a novel finding. This induction of HO-1 paralleled a decrease in intracellular GSH, and a sustained reduction in GSH resulted in a dramatic increase in HO-1. Treatment with the antioxidants N-acetyl-l-cysteine or GSH reduced the expression of HO-1 induced by CSE. We also examined the signal transduction mechanism responsible for HO-1 induction. Nuclear factor erythroid-derived 2, like 2 (Nrf2) was not involved in HO-1 induction by CSE. Activator protein-1 (AP-1) is a redox-sensitive transcription factor shown in other systems to regulate HO-1 expression. CSE exposure resulted in nuclear accumulation of c-Fos and c-Jun, two key AP-1 components. Reduction of c-Fos and c-Jun nuclear translocation by SP-600125 attenuated the CSE-induced expression of HO-1. These data support the concept that changes in the cellular redox status brought on by cigarette smoke induce HO-1 in fibroblasts. This increase in HO-1 may help protect against cigarette smoke-induced inflammation and/or cell death.

Cigarette smoke extract induces oxidative stress and apoptosis in human lung fibroblasts

2003 ◽  
Vol 284 (6) ◽  
pp. L955-L963 ◽  
Author(s):  
Stefano Carnevali ◽  
Stefano Petruzzelli ◽  
Biancamaria Longoni ◽  
Renato Vanacore ◽  
Roberto Barale ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Dna Fragmentation ◽  
Cigarette Smoke ◽  
Human Lung ◽  
Buthionine Sulfoximine ◽  
Cigarette Smoke Extract ◽  
Laser Fluorescence ◽  
Lung Fibroblasts ◽  
Confocal Laser ◽  
Human Lung Fibroblasts

Cigarette smoke is a mixture of chemicals having direct and/or indirect toxic effects on different lung cells. We investigated the effect of cigarette smoke on human lung fibroblasts (HFL-1) oxidation and apoptosis. Cells were exposed to various concentrations (1, 5, and 10%) of cigarette smoke extract (CSE) for 3 h, and oxidative stress and apoptosis were assessed by fluorescence-activated cell sorting and confocal laser fluorescence microscopy. Both oxidative stress and apoptosis exhibited a dose-response relationship with CSE concentrations. Lung fibroblasts also showed marked DNA fragmentation at the Comet assay after exposure to 10% CSE. Coincubation of HLF-1 cells with N-acetylcysteine (1 mM) during CSE exposure significantly reduced oxidative stress, apoptosis, and DNA fragmentation, whereas preincubation (3 h) with the glutathione-depleting agent buthionine sulfoximine (125 μM) produced a significant increase of oxidative stress. Cigarette smoke is a potent source of oxidative stress, DNA damage, and apoptosis for HFL-1 cells, and we speculate that this could contribute to the development of pulmonary emphysema in the lungs of smokers.

scholarly journals Differential regulation of metalloproteinase production, proliferation and chemotaxis of human lung fibroblasts by PDGF, Interleukin-1β and TNF-α

2000 ◽  
Vol 9 (3-4) ◽  
pp. 155-160 ◽  
Author(s):  
Masahiro Sasaki ◽  
Masayuki Kashima ◽  
Takefumi Ito ◽  
Akiko Watanabe ◽  
Noriko Izumiyama ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Human Lung ◽  
Lung Fibroblast ◽  
Differential Sensitivity ◽  
Lung Fibroblasts ◽  
Type I ◽  
Dependent Manner ◽  
Human Lung Fibroblast ◽  
Human Lung Fibroblasts ◽  
Tnf Α

Fibroblast migration, proliferation, extracellular matrix protein synthesis and degradation,all of which play important roles in inflammation, are them selves induced by various growth factors and cytokines. Less is known about the interaction of these substances on lung fibroblast function in pulmonary fibrosis.The goal of this study was to investigate the effects of PDGF alone and in combination with IL–1β and TNF–α on the production of human lung fibroblast matrix metalloproteinases, proliferation, and the chemotactic response. The assay for MMPs activity against FITC labeled type I and IV collagen was based on the specificity of the enzyme cleavage of collagen. Caseinolytis and gelatinolytic activities of secreted proteinases were analyzed by zymography. Fibronectin in conditioned media was measured using human lung fibronectin enzyme immunoassay. Cell proliferation was measured by 3H-Thymidine incorporation assay. Cell culture supernatants were tested for PGE2 content by ELISA. Chemotactic activity was measured using the modified Boyden chamber.Matrix metalloproteinase assay indicated that IL–1β, TNF–α and PDGF induced intestitial collagenase (MMP-1) production. MMP assay also indicated that IL–1β and TNF–α had inhibitory effects on MMP-2,9(gelatinaseA,B) production. Casein zymography confirmed that IL–1β stimulated stromlysin (matrix metalloproteinase 3; MMP–3) and gelatin zymography demonstrated that TNF–α induced MMP–9 production in human lung fibroblast, whereas PDGF alone did not. PDGF in combination with IL–1β and TNF–α induced MMP–3 and MMP–9 activity, as demonstrated by zymography. PDGF stimulated lung fibroblast proliferation in a concentration-dependent manner, whereas IL–1β and TNF–α alone had no effect. In contrast, the proliferation of human lung fibroblasts by PDGF was inhibited in the presence of IL–1β and TNF–α, and this inhibition was not a consequence of any elevation of PGE2. PDGF stimulated fibroblast chemotaxis in a concentrationdependent manner, and this stimulation was augmented by combining PDGF with IL–1β and TNF–α.These findings suggested that PDGF differentially regulated MMPs production in combination with cytokines, and further that MMP assay and zymography had differential sensitivity for detecting MMPs. The presence of cytokines with PDGF appears to modulate the proliferation and chemotaxis of human lung fibroblasts.

Cell-Cycle Changes and Oxidative Stress Response to Magnetite in A549 Human Lung Cells

2013 ◽  
Vol 26 (5) ◽  
pp. 693-702 ◽  
Author(s):  
Mathias Könczöl ◽  
Adilka Weiss ◽  
Evi Stangenberg ◽  
Richard Gminski ◽  
Manuel Garcia-Käufer ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Cycle ◽  
Stress Response ◽  
Human Lung ◽  
Oxidative Stress Response ◽  
Lung Cells ◽  
Human Lung Cells ◽  
And Oxidative Stress

scholarly journals Molecular cloning of a phosphatidylinositol-anchored membrane heparan sulfate proteoglycan from human lung fibroblasts.

1990 ◽  
Vol 111 (6) ◽  
pp. 3165-3176 ◽  
Author(s):  
G David ◽  
V Lories ◽  
B Decock ◽  
P Marynen ◽  
J J Cassiman ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Human Lung ◽  
Core Protein ◽  
Heparan Sulfate Proteoglycan ◽  
Amino Acid Sequences ◽  
Lung Fibroblasts ◽  
Sulfate Proteoglycan ◽  
Human Lung Fibroblast ◽  
Human Lung Fibroblasts ◽  
Core Proteins

Two mAbs raised against the 64-kD core protein of a membrane heparan sulfate proteoglycan from human lung fibroblasts also recognize a nonhydrophobic proteoglycan which accumulates in the culture medium of the cells. Pulse-chase studies suggest that the hydrophobic cell-associated forms act as precursors for the nonhydrophobic medium-released species. The core proteins of the medium-released proteoglycans are slightly smaller than those of the hydrophobic cell-associated species, but the NH2-terminal amino acid sequences of both forms are identical. The characterization of human lung fibroblast cDNAs that encode the message for these core proteins and the effect of bacterial phosphatidylinositol-specific phospholipase C suggest that the hydrophobic proteoglycan is membrane-anchored through a phospholipid tail. These data identify a novel membrane proteoglycan in human lung fibroblasts and imply that the shedding of this proteoglycan may be related to the presence of the phospholipid anchor.

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